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Updated: Sep 20, 2025

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
A Cyclized Helix-Loop-Helix Peptide as a Molecular Scaffold for Cell-Membrane Permeable Inhibitors for the
Daisuke Fujiwara1, Shunsuke Inaura2, Yuna Tanaka1
1Graduate School of Science, Osaka Metropolitan University, Gakuen-cho 1-1, Sakai, Osaka, 599-8531, Japan.
None:
The molecular design of inhibitors against intracellular protein-protein interactions (PPIs) is of interest for drug discovery and chemical biology. Herein, a novel cyclized helix-loop-helix (cHLH) peptide that inhibited the intracellular PPI between estrogen receptor alpha (ERα) and coactivator SRC1 are designed. The peptide, cHLH-ERα, bound to ERα and inhibited the interaction between ERα and the coactivator SRC1. Cellular imaging and yeast reporter assays showed that cHLH-ERα penetrated the cell membrane and exhibited antagonistic activity against ERα-SRC1 to inhibit the growth of a breast cancer cell.
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